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JUNDM2


Official Full Name
Jun dimerization protein 2
Organism
Homo sapiens
Gene ID
122953
Background
Enables DNA-binding transcription repressor activity, RNA polymerase II-specific and sequence-specific double-stranded DNA binding activity. Involved in negative regulation of transcription by RNA polymerase II. Part of RNA polymerase II transcription regulator complex. [provided by Alliance of Genome Resources, Feb 2025]
Synonyms
JDP2; JUNDM2

Cat.No. Product Name Price
SHH322031 shRNA set against Human JDP2 (NM_130469.3) Inquiry
SHH322035 shRNA set against Mouse JDP2 (NM_030887.2) Inquiry
SHH322039 shRNA set against Rat JDP2 (NM_053894.1) Inquiry
SHL185846 shRNA set against Rat Jundp2(NM_053894.1) Inquiry
SHL185858 shRNA set against Mouse Jundm2(NM_030887.2) Inquiry
SHW004170 shRNA set against Chicken JDP2 (NM_001277887) Inquiry
SHW006507 shRNA set against Danio rerio JDP2 (NM_001002493) Inquiry
Cat.No. Product Name Price
CDCR350193 Human JDP2 ORF Clone(NM_001135048.1) Inquiry
MiUTR1M-06192 JDP2 miRNA 3'UTR clone Inquiry
CDFR013466 Rat Jdp2 cDNA Clone(NM_053894.1) Inquiry
CDFH009525 Human JDP2 cDNA Clone(NM_001135048.1) Inquiry
CDFH009524 Human JDP2 cDNA Clone(NM_001135049.1) Inquiry
CDFH009523 Human JDP2 cDNA Clone(NM_001135047.1) Inquiry
MiUTR1R-02746 JDP2 miRNA 3'UTR clone Inquiry
MiUTR4H-TG11543 JDP2 miRNA 3'UTR clone Inquiry
CDCL122517 Human Jundm2 ORF clone (NM_030887.2) Inquiry
CDCR380653 Rat Jdp2 ORF Clone(NM_053894.1) Inquiry
CDCL122375 Mouse JDP2 ORF clone (NM_001135049.1) Inquiry
CDCH387510 Mouse JDP2 ORF clone(NM_001205053.1) Inquiry
CDCH387507 Human JDP2 ORF clone(NM_130469.3) Inquiry
CDCB193833 Rabbit JDP2 ORF clone (XM_008272030.1) Inquiry
CDCB167982 Danio rerio JDP2 ORF Clone (NM_001002493) Inquiry
CDCR350190 Human JDP2 ORF Clone(NM_001135047.1) Inquiry
CDCB165645 Chicken JDP2 ORF Clone (NM_001277887) Inquiry

Detailed Information

Recent Research

The c-Jun dimerization protein 2 (JDP2) is a member of the basic leucine zipper (bZIP) superfamily, which is part of the activator protein-1 (AP-1) family. AP-1-driven genes play crucial roles in many aspects of liver carcinogenesis, including proliferation, differentiation, and reactive oxygen species (ROS) accumulation and metabolism. Some studies have showed that JDP2 forms a homodimer or a heterodimer with other Jun members to repress the transcriptional activity of the AP-1 complex. Recent studies have suggested that JDP2 may function as a tumor suppressor through its suppressive action against the AP-1 complex, which is known to drive oncogenic signals in several human malignancies. One report showed that high expression of JDP2 was significantly correlated with smaller tumor size and early stage Hepatocellular Carcinoma (HCC). JDP2 was associated with better survival in HCC patients. This suggests that JDP2 may serve as a tumor suppressor in HCC.

JDP2 is expressed in various kinds of cells. It was originally isolated based on its association with c-Jun3, which is a component of the transcription factor AP-1, and ATF2 (activating transcription factor 2). JDP2specifically interacts with c-Jun and ATF2. JDP2 typically suppresses transcription through binding to CRE (cAMP responsive promoter element) and TRE (trans-activator response element) DNA elements found in the promoters of numerous genes by recruitment of histone deacetylases (HDACs). DNA binding was enhanced after dimerization with c-jun, but transcription was inhibited. JDP2 inhibits transcription by multiple mechanisms. Importantly, JDP2 can act as a transcriptional activator depending on the protein binding partner, specifically with the bZIP family member CHOP10 or serve as co-activator when associates with members of the steroid hormone receptor family.

JDP2 is involved in cell differentiation processes, such as adipocytes, differentiation of skeletal muscle cells and osteoclasts. Potentiation of cell differentiation is facilitated by the ability of JDP2 to induce cell cycle withdrawal. Several studies suggest that JDP2 has a dual role in malignant transformation. On the one hand, JDP2 can counteract AP-1 transcription, and thus may interfere with the oncogenic properties of c-Jun. Indeed, JDP2 expression was found to inhibit cell transformation induced by Ras in vitro and in prostate cancer xenografts injected into SCID mice. In addition, some reports showed that JDP2 suppresses cell cycle progression by down-regulation of cyclin-A2. On the other hand, JDP2 has been identified as a candidate oncogene in a high-throughput screen based on viral insertional mutagenesis in mice. Consistently, tetracycline regulated transgenic mice expressing JDP2 in liver tissue exhibited higher mortality rate and increased number and size of tumors when compared with their wild-type counterparts in hepatocellular carcinoma mouse model. Furthermore, one report showed that JDP2 expression in the host suppresses primary tumor growth. However, it promotes metastatic spread. These metastatic effects are partially mediated by BMDCs colonizing the primary tumor site and further secreting the prometastatic chemokine, CCL5.

References:

  1. Kalfon R, et al. c-Jun dimerization protein 2 (JDP2) deficiency promotes cardiac hypertrophy and dysfunction in response to pressure overload. International Journal of Cardiology, 2017, 249.
  2. Barbarov Y, et al. Host JDP2 expression in the bone marrow contributes to metastatic spread. Oncotarget, 2015, 6(35):37737-37749.
  3. Heger J, et al. JDP2 overexpression provokes cardiac dysfunction in mice. Scientific Reports, 2018,8.
  4. Chen Y L, et al. The expression of a tumor suppressor gene JDP2 and its prognostic value in hepatocellular carcinoma (HCC) patients. Human Pathology, 2017, 63:212-216.
  5. Jonak C R, et al. c-JUN Dimerization Protein 2 (JDP2) Is a Transcriptional Repressor of Follicle-stimulating Hormone β (FSHβ) and Is Required for Preventing Premature Reproductive Senescence in Female Mice. Journal of Biological Chemistry, 2017, 292(7):2646.
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